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Structure and Intrinsic Disorder in Enzymology

  • 1st Edition - November 17, 2022
  • Latest edition
  • Editors: Munishwar Nath Gupta, Vladimir N. Uversky
  • Language: English

Structure and Intrinsic Disorder in Enzymology offers a direct, yet comprehensive presentation of the fundamental concepts, characteristics and functions of intrinsically disordere… Read more

Description

Structure and Intrinsic Disorder in Enzymology offers a direct, yet comprehensive presentation of the fundamental concepts, characteristics and functions of intrinsically disordered enzymes, along with valuable notes and technical insights powering new research in this emerging field. Here, more than twenty international experts examine protein flexibility and cryo-enzymology, hierarchies of intrinsic disorder, methods for measurement of disorder in proteins, bioinformatics tools for predictions of structure, disorder and function, protein promiscuity, protein moonlighting, globular enzymes, intrinsic disorder and allosteric regulation, protein crowding, intrinsic disorder in post-translational, and much more.

Chapters also review methods for study, as well as evolving technology to support new research across academic, industrial and pharmaceutical labs.

Key features

  • Unifies the roles of intrinsic disorder and structure in the functioning of enzymes and proteins
  • Examines a range of enzyme and protein characteristics, their relationship to intrinsic disorder, and methods for study
  • Features chapter contributions from international leaders in the field

Readership

Basic and translational researchers in biochemistry, biotechnology, molecular biology, cellular biology, genetics, pathology, chemistry, and pharmaceutical science; life science researchers; developmental biologists; clinicians and graduate students in the biosciences

Table of contents

1. Enzymology: Early insights
M N Gupta and Vladimir N. Uversky

2. Deep mutational scanning to probe specificity determinants.
Raghavan Varadarajan

3. Protein flexibility and cryo-enzymology: The trade-off between stability andcatalytic rates
Vladimir N. Uversky and Munishwar Gupta

4. Thermodynamic Perspective of Protein Disorder and Phase Separation: Model Systems
B. Montgomery Pettitt Pettitt

5. Structure and disorder: Protein functions depend on this new binary transforming lock-and-key into structure-function continuum
Vladimir N. Uversky and M N Gupta

6. Methods for measuring structural disorder in proteins
Sonia Longhi

7. Prediction of protein structure and intrinsic disorder in the era of deep learning
Zsuzsanna Dosztányi

8. Roles of Intrinsically Disordered Regions in Phosphoinositide 3-Kinase Biocatalysis
Vrushank Dave

9. Many faces of protein promiscuity: Not just broad specificity of proteins
M N Gupta and Vladimir N. Uversky

10. Role Of Plasticity And Disorder In Protein Moonlighting: Blurring Of Lines Between Biocatalysts And Other Biologically Active Proteins
M N Gupta and Vladimir N. Uversky

11. Molten globular enzymes
Vladimir N. Uversky

12. Intrinsic disorder and allosteric regulation
Zhirong Liu

13. Macromolecular Crowding: How it Affects Protein Structure, Disorder, and Catalysis
M N Gupta and Vladimir N. Uversky

14. Intrinsic disorder and post-translational modifications: An evolutionary perspective
Paul M. Harrison

15. The roles of prion-like domains in amyloid formation, phase separation, and solubility
Eric D. Ross

16. IDPRs of membrane proteins influence membrane curvature
Jeanne Stachowiak

17. How binding to surfaces affects disorder.
Diego Masone

Product details

  • Edition: 1
  • Latest edition
  • Published: November 17, 2022
  • Language: English

About the editors

MG

Munishwar Nath Gupta

Dr. Munishwar Nath Gupta earned his PhD from Indian Institute of Science, Bengaluru, and completed post-doctoral positions at Massachusetts Institute of Technology (USA), University of Minnesota (USA), Lund University (Sweden), and University of Technology of Compiegne (France). He has taught chemistry, biochemistry, and biotechnology at the Indian Institute of Technology, Delhi, between 1975-2016. He was awarded the National Science Talent fellowship (India) and Fellowships of National Academy of Sciences and Indian National Science Academy. He has edited three books on thermostability of enzymes, non-aqueous enzymology and affinity-based separation methods. He was an Associate Editor of Biocatalysis and Biotransformation (Taylor and Francis) and the founding and former editor-in-chief of Sustainable Chemical Processes (Springer). He’s served on editorial boards of several national and international journals and acted as a consultant to Novozyme (Denmark), Dabur (India), and other international companies.
Affiliations and expertise
Former Emeritus Professor, Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology, Delhi, India

VU

Vladimir N. Uversky

Vladimir N. Uversky is Professor in the Department of Molecular Medicine at the Morsani College of Medicine, University of South Florida. His research centers on protein folding, misfolding, and intrinsic disorder. He began his career at the Institute of Protein Research and the Institute for Biological Instrumentation in Russia, before moving to the University of California, Santa Cruz in 1998 and Indiana University–Purdue University Indianapolis in 2004, where he served as Senior Research Professor. He has been at USF since 2010 and is a Fellow of the Royal Society of Biology, the Royal Society of Chemistry, and the American Institute for Medical and Biological Engineering. Professor Uversky co-founded the Intrinsically Disordered Proteins Subgroup at the Biophysical Society and the Intrinsically Disordered Proteins Gordon Research Conference, and has edited several books and book series on protein structure, folding, and misfolding. He serves as an editor for several scientific journals.

Affiliations and expertise
PhD, DSc, FRSB, FRSC, FAIMBE, Professor at the Department of Molecular Medicine, Morsani College of Medicine, University of South Florida

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